Controlling Polymer Structure with Precise Sequence Design

Optimal polymer design is challenging due to the vastness of polymeric chemical and structural possibilities. This work provides atomic-level insight to establish simple design rules to control polymer structure through precise sequencing. We use sequence-specific polypeptoids, whose structural effects can be studied with experimental and simulation techniques to explore how monomer sequences can impact polymer folding and assembly. Specifically, two model systems are studied to examine changes in the local and global structure of the polypeptoid chains. To explore these effects, we simulate polypeptoid chains in solution to understand how the number and location of the hydrophobic and chiral monomers lead to changes in their structural ensemble. The number and position of chiral centers alters local peptoid helical formation. Furthermore, global polymer structure is controlled by leveraging the role of hydrophobicity. These computational methods will provide a molecular insight into the driving forces for polymer conformation and guide the development of new materials with tunable properties.